Myosin subfragment

Rayment, 1., et al. Three-dimensional structure of myosin subfragment-1 a molecular motor. Science 261 5-58, 1996. 

Myosin Subfragment-1 Interacts With Two G-Actin Molecules... 

Combeau, C., Didry, D., Carlier. M.-F. (1992). Interaction between G-actin and myosin subfragment-I probed by covalent crosslinking. J. Biol. Chem. 267, 14038-14046. 

Fievez, S. Carlier, M.-F. (1993). Conformational changes in subdomain-2 of G-actin upon polymerization into F-actin and upon binding myosin subfragment-1. FEES Lett. 316, 186-190. 

Miller, L., Phillips, M Reisler, E. (1988). Polymerization of G-actin by myosin subfragment-1. J. Biol. Chem. 263, 1996-2002. 

Figure 14. Crystal structures of actin and myosin subfragment-1, shown to the same scale.

Miki M, Dosremedios CG (1988) Fluorescence quenching studies of fluorescein attached to Lys-61 or Cys-374 in actin effects of polymerization, myosin subfragment-1 binding, and tropomyosin-troponin binding. J Biochem Tokyo 104 232-235... 

Iodoacetyl-LC-biotin has been used to localize the SH thiol of myosin by use of an avidin-biotin complex visualized by electron microscopy (Sutoh et al., 1984) and to determine the spatial relationship between SHj and the actin binding site on the myosin subfragment-1 surface (Yamamoto et al., 1984). 

Aguirre, R., Gonsoulin, F., and Cheung, H.C. (1986) Interaction of fluorescently labelled myosin subfragment 1 with nucleotide and actin. Biochemistry 25, 6827. 

Greene, L.E. (1986) Cooperative binding of myosin subfragment one to regulated acdn as measured by fluoresce changes of troponin 1 modified within different fluorophores./. Biol. Chem. 261, 1279. 

Labbe, J.R, Mornet, D., Roseau, G., and Kassab, R. (1982) Cross-linking of F-actin to skeletal muscle myosin subfragment 1 with bis(imido esters) Further evidence for the interaction of myosin-head heavy chain with an actin dimer. Biochemistry 21, 6897-6902. 

Sutoh, K., and Hiratsuka, T. (1988) Spatial proximity of the glycine-rich loop and the SH2 thiol in myosin subfragment 1. Biochemistry 27(8), 2964-2969. 

Wells, J.A., Knoeber, C., Sheldon, M.C., Werber, M.M., and Yount, R.G. (1980) Cross-linking of myosin subfragment 1. Nucleotide-enhanced modification by a variety of bifunctional reagents./. Biol. Chem. 255, 11135. 

Yamamoto, K., Sekine, T., and Sutoh, K. (1984) Spatial relationship between SHI and the actin binding site on myosin subfragment-1 surface. FEES Lett. 176, 75-78. 

White et aP measured the rates of phosphate release during a single turnover of actomyosin nucleoside triphosphate (NTP) hydrolysis using a double-mixing stopped-flow spectrofluorometer, at very low ionic strength to increase the affinity of myosin-ATP and myo-sin-ADP-Pi to actin. Myosin subfragment 1 and a series of nucleoside triphosphates were mixed and incubated for approximately 1-10 s to allow NTP to bind to myosin and generate a steady-state mixture of myosin-NTP and myosin-NDP-Pi. The steady-state intermediates were then mixed with actin. 

Figure 19-15 Ribbon representation of chicken skeletal myosin subfragment-1 showing the major domains and tryptic fragments. Prepared with the program MolScript. From Rayment.157...

Houdusse, A., Kalabokis, V. N., Himmel, D., Szent-Gyorgyi, A. G., and Cohen, C. (1999). Atomic structure of scallop myosin subfragment SI complexed with MgADP A novel conformation of the myosin head. Cell 97, 459-470. 

Rayment, I., Rypniewski, W. R., Schmidt-Base, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., and Holden, H. M. (1993b). Three-dimensional structure of myosin subfragment-1 A molecular motor. Science 261, 50-58. 

Lehrer, S. S., Golitsina, N. L., and Geeves, M. A. (1997). Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions. Biochemistry 36, 13449-13454. 

McKillop, D. F., and Geeves, M. A. (1991). Regulation of the acto.myosin subfragment 1 interaction by troponin/tropomyosin. Evidence for control of a specific isomerization between two acto.myosin subfragment 1 states. Biochem. J. 279(Pt3), 711-718. 

Criddle, A. H., Geeves, M. A., andjeffries, T. (1985). The use of actin labeled with N-(l-pyrenyl)iodoacetamide to study the interaction of actin with myosin subfragments and troponin/tropomyosin. Biochem. J. 232, 343-349. 

Millar, N. C., and Geeves, M. A. (1983). The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1. FEES Lett. 160, 141-148. 

Urbanke, C., and Wray, J. (2001). A fluorescence temperature-jump study of conformational transitions in myosin subfragment 1. Biochem.J. 358, 165—173. 

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